2018-09-28

2018-06-02

2018-04-02

2018-03-14

2017-08-23

2017-04-07

EGFR·EGFè¤åä½

Epidermal growth factor (EGF) regulates cell proliferation and differentiation by binding to the EGF receptor (EGFR) extracellular region, comprising domains I-IV, with the resultant dimerization of the receptor tyrosine kinase. In this study, the crystal structure of a 2:2 complex of human EGF and the EGFR extracellular region has been determined at 3.3 &Aring; resolution. EGFR domains I-III are arranged in a C shape, and EGF is docked between domains I and III. The 1:1 EGF&middot;EGFR complex dimerizes through a direct receptor*receptor interaction, in which a protruding &beta;-hairpin arm of each domain II holds the body of the other. The unique "receptor-mediated dimerization" was verified by EGFR mutagenesis.